User:Joanne Lau/sandbox 2

One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

Molecular Playground banner: "ClpX ‘spring cleans’ by dumping some proteins and refolding others. More at MolecularPlayground.org."

Intro 

Asymmetry

320-416

large AAA+ domain 61-314

linkers 315-319

angle_ClpX_noNucleotide

angle_ClpX_noNucleotide_label

angle_ClpX_boundNucleotide

TextToBeDisplayed

chain label

Unusual Structural Features of Hexameric ClpX
Central Pore of the Hexameric ClpX is Conserved, Asymmetry, Falls into two classes of subunits

How ClpX Recognizes Specific Proteins
Itself can recognize proteins with certain motifs. Adaptors enhance reactivity, sspB, Rssb.

Hexameric ClpX Unfolds and Drives Proteins Through its Aperture
Angle changes and height changes, pulling a protein through to unfold it

Interaction between ClpX and ClpP results in a powerful Protein Degradation Machinery
Interaction between ClpX and ClpP donut in a row, which domain interacts. Critical to determine ClpX role as a chaperone or a protease. How powerful

References